Advanced SearchSearch Tips
Evaluation of Salt, Microbial Transglutaminase and Calcium Alginate on Protein Solubility and Gel Characteristics of Porcine Myofibrillar Protein
facebook(new window)  Pirnt(new window) E-mail(new window) Excel Download
 Title & Authors
Evaluation of Salt, Microbial Transglutaminase and Calcium Alginate on Protein Solubility and Gel Characteristics of Porcine Myofibrillar Protein
Hong, Geun-Pyo; Chin, Koo-Bok;
  PDF(new window)
Response surface methodology was adopted to model and optimize the effects of microbial transglutaminase (TG) and calcium alginate (CA) systems of various ratios on the gelation characteristics of porcine myofibrillar protein (MP) at various salt levels. The CA system consisting of sodium alginate (SA), calcium carbonate (CC) and glucono--lactone (GdL) showed no remarkable changes in the salt-soluble fraction, and only minor effects on electrostatic interactions were observed. Increasing CA concentration caused acid-induced hydrophobic interactions in MPs, resulting in increased MP gel strength. The TG system, containing TG and sodium caseinate (SC), induced cold-set MP gelation by formation of covalent bonding. The main advantage of the combined system was a higher cooking yield when the MP gel was heated. These results indicated that 0.7% TG combined with 0.8% CA system can form a viscoelastic MP gel, regardless of salt levels.
Microbial transglutaminase;calcium alginate;myofibrillar protein;gel characteristics;
 Cited by
Evaluation of red bean protein [Vigna angularis] isolate on rheological properties of pork myofibrillar protein gels induced by microbial transglutaminase, International Journal of Food Science & Technology, 2015, 50, 7, 1583  crossref(new windwow)
Boles, J. A. and Shand P. J. (1998) Effect of comminution method and raw binder system in restructured beef. Meat Sci. 49, 297-307. crossref(new window)

Bryant, C. M. and McClements, D. J. (1998) Molecular basis of protein functionality with special consideration of cold-set gels derived from heat-denatured whey. Trend Food Sci. Technol. 9, 143-151. crossref(new window)

Chin, K. B., Go, M. Y., and Xiong, Y. L. (2009a) Konjac flour improved textural and water retention properties of transglutaminase-mediated, heat-induced porcine myofibrillar protein gel: Effect of salt level and transglutaminase incubation. Meat Sci. 81, 565-572. crossref(new window)

Chin, K. B., Go, M. Y., and Xiong, Y. L. (2009b) Effect of soy protein substitution for sodium caseinate on the transglutaminase- induced cold and thermal gelation of myofibrillar protein. Food Res. Int. 42, 941-948. crossref(new window)

Cochran, W. G. and Cox, G. M. (1992) Experimental designs, 2nd edn. John Wiley and Sons Inc., NY, pp 335-375.

Draget, K. I., Ostgaard, K., and Smidsrod, O. (1991) Homogeneous alginate gels: A technical approach. Carbohydr. Polym. 14, 159-178.

Fernandez-Martin, F., Cofrades, S., Carballo, J., and Jimenez-Colmenero, F. (2002) Salt and phosphate effects on the gelling process of pressure/heat treated pork batters. Meat Sci.61, 15-23. crossref(new window)

Folk, J. E. (1980). Transglutaminase. Ann. Rev. Biochem. 49, 517-531. crossref(new window)

Gornall, A. G., Bardawill, C. Y., and David, M. M. (1949) Determination of serum proteins by means of the biuret reaction. J. Biol. Chem. 177, 751-766.

Hong, G. P. and Chin, K. B. (2009) Optimisations of calcium alginate and microbial transglutaminase systems to form a cold-set myofibrillar protein gelation. Korean J. Food Sci. Ani. Resour. 5, 590-598. crossref(new window)

Hong, G. P. and Chin, K. B. (2010a) Effects of microbial transglutaminase and sodium alginate on cold-set gelation of porcine myofibrillar protein with various salt levels. Food Hydrocolloid. 24, 444-451. crossref(new window)

Hong, G. P. and Chin, K. B. (2010b) Evaluation of sodium alginate and glucono-$\delta$-lactone levels on the cold-set gelation of porcine myofibrillar protein at different salt concentrations. Meat Sci. 85, 201-209. crossref(new window)

Kulmyrzaev, A., Chanamai, R., and McClements, D. J. (2000) Influence of pH and $CaCl_{2}$ on the stability of dilute whey protein stabilized emulsions. Food Res. Int. 33, 15-20. crossref(new window)

Kuraish, C., Sakamoto, J., Yamazaki, K., Susa, Y., Kuhara, C., and Soeda, T. (1997) Production of restructured meat using microbial transglutaminase without salt or cooking. J. Food Sci. 62, 488-490, 515. crossref(new window)

Kutemeyer, C., Froeck, M., Werlein, H. D., and Watkinson, B. M. (2005) The influence of salts and temperature on enzymatic activity of microbial transglutaminase. Food Control. 16, 735-737. crossref(new window)

Lee, W. C., Yusof, S., Hamid, N. S. A., and Baharin, B. S. (2006) Optimizing conditions for enzymatic clarification of banana juice using response surface methodology (RSM). J. Food Eng. 73, 55-63. crossref(new window)

Mancini, M., Moresi, M., and Rancini, R. (1999) Mechanical properties of alginate gels: empirical characterization. J. Food Eng. 39, 369-378. crossref(new window)

McClements, D. J. (1999) Food emulsions: Principles, practice, and techniques. CRC Press, Boca Raton, pp. 17-37.

McClements, D. J. (2006) Non-covalent interactions between proteins and polysaccharides. Biotechnol. Adv. 24, 621-625. crossref(new window)

Means, W. J. and Schmidt, G. R. (1986) Algin/calcium gel as a raw and cooked binder in structured beef steaks. J. Food Sci. 51, 60-65. crossref(new window)

Means, W. J. and Schmidt, G. R. (1987) Restructuring fresh meat without the use of salt or phosphate. In: Advanced in meat research. Pearson, A. M. and Dutson, T. R. (eds.) Van Nostrand Reinhold, NY, Vol. 3, pp. 469-487.

Moreno, H. M., Carballo, J., and Borderias, A. J. (2008) Influence of alginate and microbial transglutaminase as binding ingredients on restructured fish muscle processed at low temperature. J. Sci. Food Agric. 88, 1529-1536. crossref(new window)

Neiser, S., Draget, K. I., and Smidsrod, O. (1999) Interactions in bovine serum albumin-calcium alginate gel systems. Food Hydrocolloid. 13, 445-458. crossref(new window)

Ngapo, T. M., Wilkinson, B. H. P., and Chong, R. (1996) 1,5-Glucono-a-lactone-induced gelation of myofibrillar protein at chilled temperature. Meat Sci. 42, 3-13. crossref(new window)

Nielsen, G. S., Petersen, B. R., and Moller, A. J. (1995) Impact of salt, phosphate and temperature on the effects of a transglutaminase (F XIIIa) on the texture of restructured meat. Meat Sci. 41, 293-99. crossref(new window)

Park, J. W. (2000) Ingredient technology and formulation development. In: Surimi and surimi seafood. Park, J. W. (ed.) Marcel Dekker Inc., NY, pp. 343-391.

Ramirez, J., Uresti, R., Tellez, S., and Vazquez, M. (2002) Using salt and microbial transglutaminase as binding agents in restructured fish products resembling hams. J. Food Sci. 67, 1778-1784. crossref(new window)

Ramirez-Suarez, J. C. and Xiong, Y. L. (2003) Effect of transglutaminase-induced cross-linking on gelation of myofibrillar/soy protein mixtures. Meat Sci. 65, 899-907. crossref(new window)

Sakamoto, H., Kumazawa, Y., and Motoki, M. (1994) Strength of protein gels prepared with microbial transglutaminase as related to reaction conditions. J. Food Sci. 59, 866-871. crossref(new window)

Xiong, Y. L. (1993) A comparison of the rheological characteristics of different fractions of chicken myofibrillar proteins. J. Food Biochem. 16, 217-227.